eF-site ID 1e55-AB PDB Code 1e55 Chain A, B click to enlarge Title Crystal structure of the inactive mutant Monocot (Maize ZMGlu1) beta-glucosidase ZMGluE191D in complex with the competitive inhibitor dhurrin Classification HYDROLASE Compound BETA-GLUCOSIDASE Source (BGLC_MAIZE) Sequence A:  VQMLSPSEIPQRDWFPSDFTFGAATSAYQIEGAWNEDGKG ESNWDHFCHNHPERILDGSNSDIGANSYHMYKTDVRLLKE MGMDAYRFSISWPRILPKGTKEGGINPDGIKYYRNLINLL LENGIEPYVTIFHWDVPQALEEKYGGFLDKSHKSIVEDYT YFAKVCFDNFGDKVKNWLTFNDPQTFTSFSYGTGVFAPGR CSPGLDCAYPTGNSLVEPYTAGHNILLAHAEAVDLYNKHY KRDDTRIGLAFDVMGRVPYGTSFLDKQAEERSWDINLGWF LEPVVRGDYPFSMRSLARERLPFFKDEQKEKLAGSYNMLG LNYYTSRFSKNIDISPNYSPVLNTDDAYASQEVNGPDGKP IGPPMGNPWIYMYPEGLKDLLMIMKNKYGNPPIYITENGI GDVDTKETPLPMEAALNDYKRLDYIQRHIATLKESIDLGS NVQGYFAWSLLDNFEWFAGFTERYGIVYVDRNNNCTRYMK ESAKWLKEFNTA B:  MLSPSEIPQRDWFPSDFTFGAATSAYQIEGAWNEDGKGES NWDHFCHNHPERILDGSNSDIGANSYHMYKTDVRLLKEMG MDAYRFSISWPRILPKGTKEGGINPDGIKYYRNLINLLLE NGIEPYVTIFHWDVPQALEEKYGGFLDKSHKSIVEDYTYF AKVCFDNFGDKVKNWLTFNDPQTFTSFSYGTGVFAPGRCS PGLDCAYPTGNSLVEPYTAGHNILLAHAEAVDLYNKHYKR DDTRIGLAFDVMGRVPYGTSFLDKQAEERSWDINLGWFLE PVVRGDYPFSMRSLARERLPFFKDEQKEKLAGSYNMLGLN YYTSRFSKNIDISPNYSPVLNTDDAYASQEVNGPDGKPIG PPMGNPWIYMYPEGLKDLLMIMKNKYGNPPIYITENGIGD VDTKETPLPMEAALNDYKRLDYIQRHIATLKESIDLGSNV QGYFAWSLLDNFEWFAGFTERYGIVYVDRNNNCTRYMKES AKWLKEFNTA Description Functional site 1) chain A residue 402-410 type prosite sequence IYITENGIG description GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. IYITENGIG source prosite : PS00572 2) chain A residue 28-42 type prosite sequence FTFGAATSAYQIEGA description GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FtFGaAtSAYQiEgA source prosite : PS00653 3) chain A residue 191 type ACT_SITE sequence D description Proton donor => ECO:0000250|UniProtKB:Q7XKV4 source Swiss-Prot : SWS_FT_FI1 4) chain B residue 191 type ACT_SITE sequence D description Proton donor => ECO:0000250|UniProtKB:Q7XKV4 source Swiss-Prot : SWS_FT_FI1 5) chain A residue 406 type ACT_SITE sequence E description Nucleophile => ECO:0000250|UniProtKB:Q7XKV4 source Swiss-Prot : SWS_FT_FI2 6) chain B residue 406 type ACT_SITE sequence E description Nucleophile => ECO:0000250|UniProtKB:Q7XKV4 source Swiss-Prot : SWS_FT_FI2 7) chain A residue 38 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:11106394, ECO:0000305|PubMed:12684498, ECO:0007744|PDB:1E56, ECO:0007744|PDB:1H49 source Swiss-Prot : SWS_FT_FI3 8) chain B residue 38 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:11106394, ECO:0000305|PubMed:12684498, ECO:0007744|PDB:1E56, ECO:0007744|PDB:1H49 source Swiss-Prot : SWS_FT_FI3 9) chain A residue 142 type BINDING sequence H description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 10) chain A residue 190 type BINDING sequence N description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 11) chain A residue 333 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 12) chain A residue 473 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 13) chain B residue 142 type BINDING sequence H description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 14) chain B residue 190 type BINDING sequence N description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 15) chain B residue 333 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 16) chain B residue 473 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56 source Swiss-Prot : SWS_FT_FI4 17) chain A residue 406 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q9SPP9 source Swiss-Prot : SWS_FT_FI5 18) chain B residue 406 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q9SPP9 source Swiss-Prot : SWS_FT_FI5 19) chain A residue 457 type BINDING sequence W description BINDING => ECO:0000305|PubMed:11106394, ECO:0000305|PubMed:12684498, ECO:0007744|PDB:1E55, ECO:0007744|PDB:1E56, ECO:0007744|PDB:1H49 source Swiss-Prot : SWS_FT_FI6 20) chain A residue 464 type BINDING sequence E description BINDING => ECO:0000305|PubMed:11106394, ECO:0000305|PubMed:12684498, ECO:0007744|PDB:1E55, ECO:0007744|PDB:1E56, ECO:0007744|PDB:1H49 source Swiss-Prot : SWS_FT_FI6 21) chain B residue 457 type BINDING sequence W description BINDING => ECO:0000305|PubMed:11106394, ECO:0000305|PubMed:12684498, ECO:0007744|PDB:1E55, ECO:0007744|PDB:1E56, ECO:0007744|PDB:1H49 source Swiss-Prot : SWS_FT_FI6 22) chain B residue 464 type BINDING sequence E description BINDING => ECO:0000305|PubMed:11106394, ECO:0000305|PubMed:12684498, ECO:0007744|PDB:1E55, ECO:0007744|PDB:1E56, ECO:0007744|PDB:1H49 source Swiss-Prot : SWS_FT_FI6

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